Rubiscolin, a δ selective opioid peptide derived from plant Rubisco

Yang, Shao Nian; Jinsmaa, Yunden; Sonoda, Soushi; Doyama, Naomi; Lipkowski, Andrzej W.; Kawamura, Yukio; Yoshikawa, Masaaki

doi:10.1016/s0014-5793(01)03042-3

Cited by 97 publications

(83 citation statements)

References 30 publications

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“…Casomorphins (e.g., human -casomorphin-7, YPFVEPI), 2) hemorphin (YPWT) derived from hemoglobin, 7) and endomorphin-1 and 2 (YPWF-NH 2 and YPFF-NH 2 respectively) 5) containing the Tyr-Pro-aromatic amino acid sequence in these molecules, are also -selective opioid peptides, of animal origin. In contrast, opioid peptides of plant origin, such as gluten exorphin 4,8) and rubiscolin, 9,10) with the Tyr-Pro-non-aromatic amino acid sequence, are selective for the receptor. Soymorphins were the first -selective opioid peptides of plant origin to be identified.…”

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“…In contrast, the minimum effective dose of soymorphin-7 (30 mg/kg) after oral administration was Receptor binding assay was performed essentially as described previously. 4,9) The membrane from CHO-K1 cells expressed with human opioid receptor (PerkinElmer Life Sciences, Boston, MA) was used with 1 nM of [3 H]-DAMGO (American Radiolabeled Chemicals, St. Louis, MO) as a radioligand. Non-specific binding was determined in the presence of 10 mM DAMGO.…”

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“…The digest of the fragment peptide was analyzed using an HPLC system and 492 protein sequencer (Applied Biosystems), as previously described. 9) For the 7S fraction digest, the LC/MS system (Mariner, Applied Biosystems) was used. Separation was performed with a linear gradient of acetonitrile in water containing 0.1% formic acid and 0.01% trifluoroacetic acid (TFA) from 5 to 95% (v/v) for 8 min at a flow rate of 0.2 ml/min using an ODS column, YMC Pack ProC18 (50 mm Â 2:0 mm, YMC., Kyoto, Japan).…”

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Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities

Ohinata

Agui

Yoshikawa

2007

Bioscience, Biotechnology, and Biochemistry

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Based on the amino acid sequence YPFV found in the soy -conglycinin -subunit, which is common to an opioid peptide human -casomorphin-4, peptides YPF-VV, YPFVVN, and YPFVVNA were synthesized according to their primary structure. On guinea pig ileum (GPI) assay, they showed opioid activity (IC 50 = 6.0, 9.2 and 13 M respectively) more potent than humancasomorphins, and were named soymorphins-5, -6, and -7, respectively. Their opioid activities on mouse vas deferens (MVD) assay were less potent than on GPI assay, suggesting that they are selective for the opioid receptor. Human -casomorphin-4 and soymorphin-5 were released from the soy 7S fraction (-conglycinin) by the action of gastrointestinal proteases. Soymorphins-5, -6, and -7 had anxiolytic activities after oral administration at doses of 10-30 mg/kg in the elevated plus-maze test in mice.Key words: opioid peptide; opioid receptor; anxiolytic effect; soy protein; -conglycinin -subunitOpioid is a chemical substance that has morphine-like action. An opioid peptide, bovine -casomorphin-7 (YPFPGPI), isolated from casein peptone, was the first example of bioactive peptides released from food proteins.1) We have reported that human -casomorphin-4 (YPFV) and related peptides derived from human -casein also have opioid activities, though they are less potent than their bovine counterparts.2) Of three soyconglycinin subunits (, 0 , and ), 3) the -subunit has the human -casomorphin-4 sequence (YPFV). Longer peptides, YPFVV, YPFVVN, and YPFVVNA, were synthesized according to the primary structure of theconglycinin -subunit by the Fmoc strategy, and their opioid activities were tested by guinea pig ileum (GPI) and mouse vas deferens (MVD) assay, as previously described.4) All experiments were approved by the Kyoto University Ethics Committee for Animal Research Use.The peptides were found to have opioid activities on GPI assay. Figure 1 indicates the typical suppressive effect of YPFVV on electrically stimulated contractions on GPI assay. YPFVVN and YPFVVNA also dosedependently inhibited ileum contractions (data not shown). These results suggest that YPFVV, YPFVVN, and YPFVVNA have opioid activities; they were named soymorphins-5, -6, and -7 respectively. The opioid activities of synthetic peptides derived from the soyconglycinin -subunit are summarized in Table 1. The IC 50 values of soymorphins-5, -6, and -7 on GPI assay were 6.0, 9.2, and 13 mM respectively, and their opioid activities were more potent than those of humancasomorphin-4, -5, and -6 (IC 50 = 20, 14, and 25 mM, respectively). There are three types of opioid receptors: , , and . 5,6) The opioid activities of soymorphins were larger on GPI assay than those on MVD assay, suggesting that these peptides are selective for theopioid receptor. The affinities for the -opioid receptor were 17, 39, and 47 mM respectively, and the rank order of their affinities for the receptor was consistent with that of the opioid activities on GPI assay. Taking all this 1 µM 3 µM 10 µM 1 min Guinea Pig Ileum (GPI) Assay. Ileum-...

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Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities

Ohinata

Agui

Yoshikawa

2007

Bioscience, Biotechnology, and Biochemistry

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“…5) Rubiscolin (YPLDLF) is a -opioid peptide present within spinach D-ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). 6) In a step through-type passive avoidance test in mice, rubiscolin enhanced memory consolidation at an oral dose of 100 mg/kg. 7) Rubiscolin also exerted an anxiolytic-like effect in the elevated plus-maze test after its oral administration to mice at a dose of 100 mg/kg.…”

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“…1C). Rubiscolin contains a sequence that mediates its release by pepsin, 6) and we inserted an arginine residue before the first rubiscolin repeat.…”

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Accumulation of the Bioactive Peptides, Novokinin, LPYPR and Rubiscolin, in Seeds of Genetically Modified Soybean

Nishizawa

Kita

Doi

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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Secretagogue and bacteriostatic active fractions derived from a peptic hydro‐ lysate of alfalfa RuBisCO small purified subunit

Trovaslet¹,

Kapel²,

Ravallec‐Plé³

et al. 2006

J Sci Food Agric

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For the first time a purification process for small RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) subunit (SRS) was developed from an industrial by-product of alfalfa, taking advantage of its solubility at low pH. Only one protein strip (14 kDa) was clearly detected in the sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) profile of the supernatant at pH 2. The recovery of SRS was 48% by this method, with a purity estimated as 98% by densitometry and reverse phase high-performance liquid chromatography (RP-HPLC). Moreover, most polyphenolic compounds were discarded, as confirmed by spectrophotometry and RP-HPLC. SRS hydrolysis was performed for 20 h at 37• C using pepsin in ammonia/formic acid buffer at pH 3. The hydrolysate was fractionated on a Sephadex G25 column equilibrated with ethanolamine/HCl buffer. Biological activities were found in two fractions. The first fraction showed slight bacteriostatic properties against two pathogenic bacteria, Salmonella arizonae and Shigella sonnei. The second fraction, tested by radioimmunoassay (RIA), presented a secretagogue activity comparable to that of gastrin.

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Rubiscolin, a δ selective opioid peptide derived from plant Rubisco

Cited by 97 publications

References 30 publications

Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities

Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities

Accumulation of the Bioactive Peptides, Novokinin, LPYPR and Rubiscolin, in Seeds of Genetically Modified Soybean

Secretagogue and bacteriostatic active fractions derived from a peptic hydro‐ lysate of alfalfa RuBisCO small purified subunit

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